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Cloning and expression of a dehydrin-like protein from Pistacia vera L.
Year:
2005
Source of publication :
Trees - Structure and Function
Authors :
Barazani, Oz
;
.
Volume :
19
Co-Authors:
Yakubov, B., Albert Katz Dept. Dryland B., Jacob Blaustein Inst. Desert Res., Ben-Gurion University of the Negev, 84990, Israel
Barazani, O., Albert Katz Dept. Dryland B., Jacob Blaustein Inst. Desert Res., Ben-Gurion University of the Negev, 84990, Israel
Shachack, A., Albert Katz Dept. Dryland B., Jacob Blaustein Inst. Desert Res., Ben-Gurion University of the Negev, 84990, Israel, Kennedy-Leigh Ctr. for Hort. Res., Fac. Agric., Food Environ. Sci., R., Hebrew University of Jerusalem, P.O. Box 12, Rehovot, 76100, Israel, Otto Warburg Ctr. Agric. Biotech., Fac. Agric., Food Environ. Sci., R., Hebrew University of Jerusalem, P.O. Box 12, Rehovot, 76100, Israel
Rowland, L.J., Fruit Laboratory, Beltsville Agric. Research Center, Agricultural Research Service, Beltsville, MD 20705, United States
Shoseyov, O., Kennedy-Leigh Ctr. for Hort. Res., Fac. Agric., Food Environ. Sci., R., Hebrew University of Jerusalem, P.O. Box 12, Rehovot, 76100, Israel, Otto Warburg Ctr. Agric. Biotech., Fac. Agric., Food Environ. Sci., R., Hebrew University of Jerusalem, P.O. Box 12, Rehovot, 76100, Israel
Golan-Goldhirsh, A., Albert Katz Dept. Dryland B., Jacob Blaustein Inst. Desert Res., Ben-Gurion University of the Negev, 84990, Israel
Facilitators :
From page:
224
To page:
230
(
Total pages:
7
)
Abstract:
A full-length dehydrin-like cDNA clone was obtained from a Pistacia vera L. cDNA library. The clone was sequenced and it was found that the deduced protein consists of 230 amino acids with a molecular weight of 25.87 kDa. The glycine rich protein is highly hydrophilic, contains 47.4% charged amino acids and belongs to the Kn-type of dehydrins. It comprises five repetitive units, each containing the K-segment diagnostic of dehydrins, but no serine tract (S-segment) and no Y-segment. Temporally, accumulation of the dehydrin transcript coincides with accumulation of the protein, which remains high in the bud scales of the inflorescence throughout winter. The dehydrin protein accumulates in the outer leaves (scales) of the inflorescence bud and in the bark of 1-year-old stems. In the buds it is mostly concentrated in the palisade-like cells underneath the epidermis, in the bud and in the inner bark parenchyma. Immunogold labeling revealed that it is a cytoplasmic protein with no specific organellar localization. It is suggested that the dehydrin of pistachio may have a dual function, a role in drought and cold tolerances, as well as serving as a storage protein. © Springer-Verlag 2004.
Note:
Related Files :
Amino Acids
cloning
DNA
dormancy
Forestry
Nucleic acids
proteins
Transcripts
trees
Show More
Related Content
More details
DOI :
10.1007/s00468-004-0385-0
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
29904
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:50
Scientific Publication
Cloning and expression of a dehydrin-like protein from Pistacia vera L.
19
Yakubov, B., Albert Katz Dept. Dryland B., Jacob Blaustein Inst. Desert Res., Ben-Gurion University of the Negev, 84990, Israel
Barazani, O., Albert Katz Dept. Dryland B., Jacob Blaustein Inst. Desert Res., Ben-Gurion University of the Negev, 84990, Israel
Shachack, A., Albert Katz Dept. Dryland B., Jacob Blaustein Inst. Desert Res., Ben-Gurion University of the Negev, 84990, Israel, Kennedy-Leigh Ctr. for Hort. Res., Fac. Agric., Food Environ. Sci., R., Hebrew University of Jerusalem, P.O. Box 12, Rehovot, 76100, Israel, Otto Warburg Ctr. Agric. Biotech., Fac. Agric., Food Environ. Sci., R., Hebrew University of Jerusalem, P.O. Box 12, Rehovot, 76100, Israel
Rowland, L.J., Fruit Laboratory, Beltsville Agric. Research Center, Agricultural Research Service, Beltsville, MD 20705, United States
Shoseyov, O., Kennedy-Leigh Ctr. for Hort. Res., Fac. Agric., Food Environ. Sci., R., Hebrew University of Jerusalem, P.O. Box 12, Rehovot, 76100, Israel, Otto Warburg Ctr. Agric. Biotech., Fac. Agric., Food Environ. Sci., R., Hebrew University of Jerusalem, P.O. Box 12, Rehovot, 76100, Israel
Golan-Goldhirsh, A., Albert Katz Dept. Dryland B., Jacob Blaustein Inst. Desert Res., Ben-Gurion University of the Negev, 84990, Israel
Cloning and expression of a dehydrin-like protein from Pistacia vera L.
A full-length dehydrin-like cDNA clone was obtained from a Pistacia vera L. cDNA library. The clone was sequenced and it was found that the deduced protein consists of 230 amino acids with a molecular weight of 25.87 kDa. The glycine rich protein is highly hydrophilic, contains 47.4% charged amino acids and belongs to the Kn-type of dehydrins. It comprises five repetitive units, each containing the K-segment diagnostic of dehydrins, but no serine tract (S-segment) and no Y-segment. Temporally, accumulation of the dehydrin transcript coincides with accumulation of the protein, which remains high in the bud scales of the inflorescence throughout winter. The dehydrin protein accumulates in the outer leaves (scales) of the inflorescence bud and in the bark of 1-year-old stems. In the buds it is mostly concentrated in the palisade-like cells underneath the epidermis, in the bud and in the inner bark parenchyma. Immunogold labeling revealed that it is a cytoplasmic protein with no specific organellar localization. It is suggested that the dehydrin of pistachio may have a dual function, a role in drought and cold tolerances, as well as serving as a storage protein. © Springer-Verlag 2004.
Scientific Publication
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